MolNFT v1 · #118202 · protein
Rat prestin stas domain in complex with bromide
5EUS · PRESTIN,RAT prestin stas domain: “Rat prestin stas domain in complex with bromide”. X-ray diffraction, 1 ligand (BR), 2 pockets (best druggability 0.42). MolNFT v1 #118202 on GenesisL1: 3D structure, binding sites and pockets in…
- PDB
- 5EUS
- Type
- protein
- Length
- 129 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PRESTIN,RAT prestin stas domain
- UniProt
- Q9EPH0
- Ligands
- BR
- Pockets
- 2 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 36% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PRESTIN,RAT prestin stas domain | protein | 129 | 36% helix, 22% strand | Q9EPH0 |
Ligands and binding sites
- BR · Bromide ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A
- PG4 · Tetraethylene glycol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 63 | 0.42 | 0.81 | 14 | BR |
| 2 | 70 | 0.32 | 0.75 | 15 | PG4 |
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9EPH0
- Elsewhere: RCSB PDB 5EUS · PDBe 5EUS · UniProt Q9EPH0
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